PXD006574

PXD006574 is an original dataset announced via ProteomeXchange.

Title	An Evaluation of the Crystal Structure of C-terminal Truncated Apolipoprotein A-I in Solution Reveals Structural Dynamics Related to Lipid Binding
Description	Apolipoprotein (apo)A-I mediates many of the anti-atherogenic functions attributed to high density lipoprotein (HDL). Unfortunately, efforts toward a high-resolution structure of full-length apoA-I have not been fruitful, though there have been successes with deletion mutants. Recently, a C-terminal truncation (apoA-IΔ185-243) was crystallized as a dimer. The structure showed two helical bundles connected by a long, curved pair of swapped helical domains. To compare this structure to that existing under solution conditions, we applied small angle X-ray scattering and isotope-assisted chemical cross-linking to apoA-IΔ185-243 in its dimeric and monomeric forms. For the dimer, we found evidence for the shared domains and aspects of the N-terminal bundles, but not the molecular curvature seen in the crystal. We also found that the N-terminal bundles equilibrate between open and closed states. Interestingly, this movement is one of the transitions proposed during lipid binding. The monomer was consistent with a model in which the long shared helix doubles back onto the helical bundle. Combined with the crystal structure, these data offer an important starting point to understand the molecular details of HDL biogenesis.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:38:16.626.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD006574
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Diogo Borges Lima
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	Oxidation
Instrument	TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2017-05-23 05:55:08	ID requested
1	2017-05-30 07:38:08	announced
⏵ 2	2024-10-22 04:38:18	announced	2024-10-22: Updated project metadata.

10.1074/jbc.M115.706093;

10.6019/PXD006574;

Melchior JT, Walker RG, Morris J, Jones MK, Segrest JP, Lima DB, Carvalho PC, Gozzo FC, Castleberry M, Thompson TB, Davidson WS, An Evaluation of the Crystal Structure of C-terminal Truncated Apolipoprotein A-I in Solution Reveals Structural Dynamics Related to Lipid Binding. J Biol Chem, 291(10):5439-51(2016) [pubmed]

curator keyword: Biological

submitter keyword: apolipoprotein, mass spectrometry (MS), structural biology, oligomerization, small-angle X-ray scattering (SAXS),structural model

Paulo C Carvalho
contact affiliation	Computational Mass Spectrometry Group - Brazil
contact email	paulo@pcarvalho.com
lab head
Diogo Borges Lima
contact affiliation	Leibniz-Forschungsinstitut für Molekulare Pharmakologie
contact email	diogobor@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD006574
     1. Label: PRIDE project
     2. Name: An Evaluation of the Crystal Structure of C-terminal Truncated Apolipoprotein A-I in Solution Reveals Structural Dynamics Related to Lipid Binding